The enzyme catalyzes the asymmetric condensation of two molecules of delta-aminolevulinic acid to form porphobilinogen, which is the first common reaction in the biosynthesis of the tetrapyrroles. The enzyme shows a variable requirment for an essential zinc ion in different species which may indicate phylogenetic diversity in its chemical reaction mechanism. Among those enzymes that do not use the catalytic zinc, some appear to use a monovalent cation, some may use magnesium and others may not use any metal ions at all. On the other hand there is an allosteric Mg ion that is present in about 90% of the enzymes PMID15381398.
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 1338 A | MG | magnesium | magnesium | mononuclear | Structural |
| none | none | zinc | zinc | mononuclear | Electrostatic stabiliser Increases acidity Coordinates substrate |
*It refers to the MACiE reference pdb: 1gzg
| Metal/s Properties in Resting State | ||||||
| MG 1338 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| none | Resting state enzyme (1aw5) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 3 | |||||
| Notes | - | |||||
| References |
| -Erskine PT, Newbold R, Roper J, Coker A, Warren MJ, Shoolingin-Jordan PM, Wood SP, Cooper JB The Schiff base complex of yeast 5-aminolaevulinic acid dehydratase with laevulinic acid. Protein Sci. 1999 Jun;8(6):1250-6.(MEDLINE:10386874) |
| -Jaffe EK The porphobilinogen synthase catalyzed reaction mechanism. Bioorg Chem. 2004 Oct;32(5):316-25.(MEDLINE:15381398) |




